In search of radical intermediates in the reactions catalyzed by lysine 2,3-aminomutase and lysine 5,6-aminomutase

Journal of the American Chemical Society

Volumn 128, Issue 50, 2006, Pages 16004-16005

  Sandala, Gregory M ^a,b   Smith, David M ^c   Radom, Leo ^a,b  

^a UNIVERSITY OF SYDNEY   (Australia)

^b AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

^c RUDER BO KOVI INSTITUTE   (Croatia)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE 2,3 AMINOMUTASE; LYSINE 5,6 AMINOMUTASE; MUTASE; RADICAL;

ARTICLE; ELECTRON SPIN RESONANCE; ENERGY; ENZYME MECHANISM; MOLECULAR STABILITY; REACTION ANALYSIS; RING CLOSING METATHESIS; RING OPENING;

CATALYSIS; FREE RADICALS; INTRAMOLECULAR TRANSFERASES; LYSINE; MOLECULAR STRUCTURE; SUBSTRATE SPECIFICITY;

EID: 33845587345     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0668421     Document Type: Article

References (17)

1. 12; Banerjee, R. Ed.; Wiley-Interscience: New York, 1999; pp 835-857.
2. See, for example: (a) Banerjee, R. Chem. Rev. 2003, 103, 2083-2094.
3. (b) Toraya, T. Chem. Rev. 2003, 103, 2095-2127.
4. Tang, K.-H.; Casarez, A. D.; Wu, W.; Frey, P. A. Arch. Biochem. Biophys. 2003, 418, 49-54.
5. Ballinger, M. D.; Frey, P. A.; Reed, G. H. Biochemistry 1992, 31, 10782-10789.
6. Wu, W.; Lieder, K. W.; Reed, G. H.; Frey, P. A. Biochemistry 1995, 34, 10532-10537.
7. Magnusson, O. T.; Reed, G. H.; Frey, P. A. Biochemistry 2001, 40, 7773-7782.
8. For full details, see the Supporting Information.
9. Wetmore, S. D.; Smith, D. M.; Radom, L. J. Am. Chem. Soc. 2001, 123, 8678-8689.
10. (a) Lepore, B. W.; Ruzicka, F. J.; Frey, P. A.; Ringe, D. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 13819-13824.
11. (b) Berkovitch, F.; Behshad, E.; Tang, K.-H.; Enns, E. A.; Frey, P. A.; Drennan, C. L. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 15870-15875.
12. Henry, D. J.; Parkinson, C. J.; Mayer, P. M.; Radom, L. J. Phys. Chem. A 2001, 105, 6750-6756.
13. Wu, W.; Booker, S.; Lieder, K. W.; Bandarian, V.; Reed, G. H.; Frey, P. A. Biochemistry 2000, 39, 9561-9570.
14. See, for example: (a) Sandala, G. M.; Smith, D. M.; Radom, L. J. Am. Chem. Soc. 2004, 126, 8856-8864.
15. (b) Sandala, G. M.; Smith, D. M.; Coote, M. L.; Golding, B. T.; Radom, L. J. Am. Chem. Soc. 2006, 128, 3433-3444 and references therein.
16. We note that the P states in the 5,6-LAM- and 2,3-LAM-catalyzed reactions are likely to be accessible from the PH state of the substrate analogues t-4,5-DL and t-3,4-DL, respectively. See the Supporting Information for further details.
17. Of course, the question of whether LAM enzymes can tolerate such systems remains open.